Target details

Target details

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Alternative Name

B-cell Receptor Associated Protein 29

Background

Bap29 and the related protein Bap31 are endoplasmic reticulum (ER) and ER-vesicle membrane proteins and members of the B-cell receptor-associated protein family. These two proteins are highly homologous and can form homo- and heterodimers. Both Bap29 and Bap31 interact with membrane-bound immunoglobulins (mIgs), such as IgM and IgD, which with Ig-alpha/Ig-beta heterodimers form B cell antigen receptors. Binding of the Bap29/Bap31 heterodimer correlates with the ER retention of non-Ig-alpha/Ig-beta bound mIg complexes, suggesting that Bap29 and Bap31 may act as chaperones transmembrane regions of various proteins. Bap29 possesses multiple isoforms.

Application Details

Application Details

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Application Notes

Bap29 antibody can be used for the detection of Bap29 by Western blot at 0.5 – 1 µg/ml. (Optimal dilution should be determined by user.) Antibody can also be used for immunohistochemistry and ELISA and might be suited for other applications not tested so far.

Handling

Handling

This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

Handling Advice

Antibody can be stored at 4ºC, stable for one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures. During shipment, small volumes of antibody will occasionally become entrapped in the seal of the product vial. For products with volumes of 200 myl or less, we recommend gently tapping the vial on a hard surface or briefly centrifuging the vial in a tabletop centrifuge to dislodge any liquid in the container’s cap.

Storage

4 °C

Expiry Date

12 months

References

References

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Product cited in:

Schamel, Kuppig, Becker et al.: "A high-molecular-weight complex of membrane proteins BAP29/BAP31 is involved in the retention of membrane-bound IgD in the endoplasmic reticulum." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 100, Issue 17, pp. 9861-6, 2003 (PubMed).